In collaboration with Dr. Peter Byers at the University of Washington, we are trying to understand on a structural basis why some collagen type I mutations are lethal and others are not in the genetically transmitted bone disease known as Osteogenesis imperfecta. The cause of the disease has been traced to mutations in the genes that code for the alpha-1 and alpha-2 chains of the collagen type I triple helix. We are building molecular models of wild type collagen Type I to investigate the structural role of the point mutations. We have been extensively studying the protocol of the molecular dynamics simulations on the wild type collagen. Additionally, we have investigated other methods for collagen model building as well as the possible effects of packing, electrostatics, surface accessibility and contact of the sidechains.